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Review
. 2003 Sep;20(9):1325-36.
doi: 10.1023/a:1025771421906.

Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation

Eva Y Chi  1 , Sampathkumar Krishnan, Theodore W Randolph, John F Carpenter
Affiliations
Review

Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation

Eva Y Chi et al. Pharm Res. 2003 Sep.

Abstract

Irreversible protein aggregation is problematic in the biotechnology industry, where aggregation is encountered throughout the lifetime of a therapeutic protein, including during refolding, purification, sterilization, shipping, and storage processes. The purpose of the current review is to provide a fundamental understanding of the mechanisms by which proteins aggregate and by which varying solution conditions, such as temperature, pH, salt type, salt concentration, cosolutes, preservatives, and surfactants, affect this process.

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